Diffusional Mobility of the Cystic Fibrosis Transmembrane Conductance Regulator Mutant, ΔF508-CFTR, in the Endoplasmic Reticulum Measured by Photobleaching of GFP-CFTR Chimeras
TLDR
Photobleaching of the fluorescent ER lipid diOC4(3) showed that neither ER restructuring nor fragmentation during these maneuvers was responsible for the slowing and immobilization of CFTR, suggesting that the ER retention of ΔF508-CFTR is not due to restricted ER mobility.About:
This article is published in Journal of Biological Chemistry.The article was published on 2002-05-10 and is currently open access. It has received 28 citations till now. The article focuses on the topics: ER retention & Fluorescence recovery after photobleaching.read more
Citations
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Quality control in the endoplasmic reticulum
Lars Ellgaard,Ari Helenius +1 more
TL;DR: Recent progress is discussed in understanding the conformation-specific sorting of proteins at the level of ER retention and export, which is important for the fidelity of cellular functions.
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Dynamics of shear-induced ATP release from red blood cells
TL;DR: An in vitro microfluidic approach is used to investigate the dynamics of shear-induced ATP release from human RBCs with millisecond resolution and suggests a model wherein the retraction of the spectrin-actin cytoskeleton network triggers the mechanosensitive ATP release and aShear-dependent membrane viscosity controls the rate of release.
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GFP-like proteins stably accumulate in lysosomes.
TL;DR: It is demonstrated that certain GFP-like proteins expressed in the cytosol enter lysosomes possibly by an autophagy-related mechanism, but retain their fluorescence because of resistance not only to acidity but also to lysOSomal proteases.
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Cargo Capture and Bulk Flow in the Early Secretory Pathway
Charles Barlowe,Ari Helenius +1 more
TL;DR: This work has shown that the transport of newly synthesized proteins from the endoplasmic reticulum to the Golgi complex using a combination of mechanisms based on selective retention of proteins in the ER to prevent uptake into transport vesicles and on selective retrieval of proteins from post-ER compartments by retrograde vesicle transport is highly selective.
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SGCE missense mutations that cause myoclonus-dystonia syndrome impair ε-sarcoglycan trafficking to the plasma membrane: modulation by ubiquitination and torsinA
Christopher T. Esapa,Adrian James Waite,Matthew Locke,Matthew A. Benson,Michaela Kraus,R. A. Jeffrey McIlhinney,Roy V. Sillitoe,Philip W. Beesley,Derek J. Blake +8 more
TL;DR: It is demonstrated that some MDS-associated mutations in SGCE impair trafficking of the mutant protein to the plasma membrane and suggest a role for torsinA and the ubiquitin proteasome system in the recognition and processing of misfolded epsilon-sarcoglycan.
References
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Intracellular functions of N-linked glycans.
Ari Helenius,and Markus Aebi +1 more
TL;DR: The division of synthesis and processing between the ER and the Golgi complex represents an evolutionary adaptation that allows efficient exploitation of the potential of oligosaccharides.
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Aggresomes: A Cellular Response to Misfolded Proteins
TL;DR: The intracellular fate of cystic fibrosis transmembrane conductance regulator (CFTR) is investigated and it is demonstrated that undegraded CFTR molecules accumulate at a distinct pericentriolar structure which is termed the aggresome.
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Aggresomes, inclusion bodies and protein aggregation.
TL;DR: This work has suggested that, in animal cells, aggregated proteins are specifically delivered to inclusion bodies by dynein-dependent retrograde transport on microtubules and this microtubule-dependent inclusion body is called an aggresome.
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Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis
Seng H. Cheng,Richard J. Gregory,John Marshall,Sucharita Paul,David W. Souza,Gary A. White,Catherine R. O'Riordan,Alan E. Smith +7 more
TL;DR: It is proposed that the mutant versions of CFTR are recognized as abnormal and remain incompletely processed in the endoplasmic reticulum where they are subsequently degraded.
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Degradation of CFTR by the ubiquitin-proteasome pathway
TL;DR: It is shown that the degradation of both wild-type and mutant CFTR is inhibited by two potent proteasome inhibitors that induce the accumulation of polyubiquitinated forms of immature CFTR, confirming that ubiquitination is required for rapid CFTR degradation.